ID A0A3P8XE79_ESOLU Unreviewed; 1463 AA.
AC A0A3P8XE79;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Neurexin 1b {ECO:0000313|Ensembl:ENSELUP00000001372.2};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000001372.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000001372.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000001372.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the neurexin family.
CC {ECO:0000256|ARBA:ARBA00010241}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR Ensembl; ENSELUT00000017489.2; ENSELUP00000001372.2; ENSELUG00000002964.2.
DR GeneTree; ENSGT00940000154292; -.
DR Proteomes; UP000265140; LG05.
DR Bgee; ENSELUG00000002964; Expressed in brain and 7 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00110; LamG; 6.
DR Gene3D; 2.60.120.200; -; 6.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR003585; Neurexin-like.
DR InterPro; IPR027789; Syndecan/Neurexin_dom.
DR PANTHER; PTHR15036:SF49; AXOTACTIN; 1.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 6.
DR Pfam; PF01034; Syndecan; 1.
DR SMART; SM00294; 4.1m; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00282; LamG; 6.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 6.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS50025; LAM_G_DOMAIN; 6.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000265140};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..1463
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5027939876"
FT TRANSMEM 1390..1410
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..212
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 208..246
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 263..445
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 452..646
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 650..687
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 692..876
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 867..1044
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1047..1084
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1088..1288
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 1293..1380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1430..1463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1447..1463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1463 AA; 160332 MW; 532C8C0A325940EB CRC64;
MCLRVCVMAV CVWAAAPLLC VWLCLCSIGG SRGEVLEFGG VSGQWGRFPV WNACCESVLS
FRVKTHSEDG LLLYLDDEGF CDFLELLLLR GKLRLRFSIF CAEPAEVSSG VAVSDGHWHE
VRVKRDWRNT SLEVDERMEG WAEVKSKRRD MTVFSHTFMG GVSPELHASP LRLTSPGVRD
HKPFSGWLTE VTVNGSAVVL EASEGVTKGD GCGPDHVCQN GGLCSVIEHR AICDCTHTGY
KGNDCSEGLA HLMIGDQARE DYVATFKGSE YFCYDLSPSP IQSSSDEITL SFKTLQRNGL
MLHTGKSADY VNLALKNGAV SLVINLGSGA FEALVEPVNG KFNDNAWHDV KVTRNLRQVT
ISVDGILTTT GYTQEDYTML GSDDFFYVGG SPSTADLPGS PVSNNFMGCL KEVVYKNNDV
RLELSRLAKQ GDAKMKVSGV VAFKCESVAT LDPVTFDTPE SFVALSKWSA KKAGSISFDF
RTTEPNGLML FSHGKQRQQQ RKDPRTPPTV KVDFFAIEML DGHLYLLLDM GSGTTKTKAI
DRKVNDGEWY HVDFQRDGRS GTISVNSQRT AYTAPGDSEI LDLDDTLYLG GLPEDRQGLI
FPTEVWTALL NYGYVGCVRD LFVDGQSKDI RRLAEAQRAV GVKPSCSREP PKQCLSNPCQ
HSATCREGWN RYVCDCSGTG YLGRACERDA TILSYDGSKF MKVQLPVAMH TEAEDVSLRF
RSQRAYGVLM ATTSRNSADT LRLELDGGRV RLTVNLDCIR INCTTSKGPE TIFSGVGLND
NEWHTVRVVR RGKSLKLTVD DLQPVEGQMA GDHTQLEFHN VETGIVTEKR FMPAVPSNFI
GHLQGLTLNG MPYIDLCKNT QLTLTHTVRH SVPTHCWVLA DRPRFIHTPY LTARTIDLAA
RLETHDSSLV LWILGKNGDI DYCDYLHYVS DLGNGAHLIK GNSNSPLNDN HWHNVLISRD
TNNLHTVKID TKVTTQTTMG AKNLDLKGDL YVGGVAKEMY RDLPKLVHSR EGFQGCLATV
DLNGRLPDLL ADALATTGQV ERGCEGPSTT CQEDSCSNQG VCLQQWEGFS CDCSMTSFGG
PLCNDAGTTY IFGRDGGVIV YTWPPNERPS TRADRLALGF STQQKHATLL RVDSASGLGD
YLQLQIDKGN IRVVFNVGTD DINIEETAKF VNDGKYHIVR FTRSGGNATL QLDDLPVIER
YPSGNIDNER LAIARQRIPY RLGRVVDDWL LDKGRQLTIF NSQTTVTVGG GQGAGPFQGQ
MAGLYYNGLK ILNMAAEGHA HIRLEGSTRL VGDMPSSSIT PQSSAAAGGN RSDPVANAGD
ITTTTATNRK QGGGTTQQST DDLLVASAEC PSDDEDIDPC DPTAQPPLPD VKPFPGTSEV
VRESSSTTGM VVGIVAAAAL CILILLYAMY KYRNRDEGSY HVDESRNYIS NSATQPNGSA
KDKPLGIAKI SKNKKNKDKE YYV
//
